ID A0A0Q9ZJL6_9GAMM Unreviewed; 719 AA. AC A0A0Q9ZJL6; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 15-FEB-2017, entry version 11. DE RecName: Full=Fatty acid oxidation complex subunit alpha {ECO:0000256|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase {ECO:0000256|HAMAP-Rule:MF_01621}; DE EC=4.2.1.17 {ECO:0000256|HAMAP-Rule:MF_01621}; DE EC=5.1.2.3 {ECO:0000256|HAMAP-Rule:MF_01621}; DE EC=5.3.3.8 {ECO:0000256|HAMAP-Rule:MF_01621}; DE Includes: DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01621}; DE EC=1.1.1.35 {ECO:0000256|HAMAP-Rule:MF_01621}; GN Name=fadB {ECO:0000256|HAMAP-Rule:MF_01621, GN ECO:0000313|EMBL:KRG32409.1}; GN ORFNames=AK822_12715 {ECO:0000313|EMBL:KRG32409.1}; OS Psychrobacter sp. P11F6. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Moraxellaceae; Psychrobacter. OX NCBI_TaxID=1699621 {ECO:0000313|EMBL:KRG32409.1, ECO:0000313|Proteomes:UP000050989}; RN [1] {ECO:0000313|EMBL:KRG32409.1, ECO:0000313|Proteomes:UP000050989} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P11F6 {ECO:0000313|EMBL:KRG32409.1, RC ECO:0000313|Proteomes:UP000050989}; RA Ruckert C., Albersmeier A., Moghadam M.S., Winkler A., Lale R., RA Kalinowski J.; RT "High quality draft genome sequence of Psychrobacter sp. P11F6, RT isolated from an ascidian tunicate in the Norwegian sea."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the aerobic and anaerobic degradation of CC long-chain fatty acids via beta-oxidation cycle. Catalyzes the CC formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. CC It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as CC substrate. {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00079501}. CC -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl- CC CoA + H(2)O. {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00649301}. CC -!- CATALYTIC ACTIVITY: (3Z)-dodec-3-enoyl-CoA = (2E)-dodec-2-enoyl- CC CoA. {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00079430}. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA CC + NADH. {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00649760}. CC -!- CATALYTIC ACTIVITY: (S)-3-hydroxybutanoyl-CoA = (R)-3- CC hydroxybutanoyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00079425}. CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation. CC {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00649747}. CC -!- SUBUNIT: Heterotetramer of two alpha chains (FadB) and two beta CC chains (FadA). {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00079502}. CC -!- SIMILARITY: In the C-terminal section; belongs to the 3- CC hydroxyacyl-CoA dehydrogenase family. {ECO:0000256|HAMAP- CC Rule:MF_01621, ECO:0000256|SAAS:SAAS00556605}. CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA CC hydratase/isomerase family. {ECO:0000256|HAMAP-Rule:MF_01621, CC ECO:0000256|SAAS:SAAS00649310}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01621}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KRG32409.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LJCE01000002; KRG32409.1; -; Genomic_DNA. DR RefSeq; WP_060491905.1; NZ_CM003594.1. DR EnsemblBacteria; KRG32409; KRG32409; AK822_12715. DR UniPathway; UPA00659; -. DR Proteomes; UP000050989; Chromosome. DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro. DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004165; F:dodecenoyl-CoA delta-isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway. DR Gene3D; 1.10.1040.10; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.226.10; -; 1. DR HAMAP; MF_01621; FadB; 1. DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS. DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd. DR InterPro; IPR006108; 3HC_DH_C. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR001753; Crotonase_core_superfam. DR InterPro; IPR012799; FadB. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00725; 3HCDH; 1. DR Pfam; PF02737; 3HCDH_N; 1. DR Pfam; PF00378; ECH_1; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52096; SSF52096; 1. DR TIGRFAMs; TIGR02437; FadB; 1. DR PROSITE; PS00067; 3HCDH; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000050989}; KW Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01621, KW ECO:0000256|SAAS:SAAS00649724}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01621, KW ECO:0000256|SAAS:SAAS00649311, ECO:0000313|EMBL:KRG32409.1}; KW Lipid degradation {ECO:0000256|HAMAP-Rule:MF_01621, KW ECO:0000256|SAAS:SAAS00051736}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01621, KW ECO:0000256|SAAS:SAAS00649712}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00649306, KW ECO:0000313|EMBL:KRG32409.1}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01621, KW ECO:0000256|SAAS:SAAS00649309}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01621, ECO:0000256|SAAS:SAAS00649745}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01621, KW ECO:0000256|SAAS:SAAS00649305, ECO:0000313|EMBL:KRG32409.1}. FT DOMAIN 318 496 3HCDH_N. {ECO:0000259|Pfam:PF02737}. FT DOMAIN 498 593 3HCDH. {ECO:0000259|Pfam:PF00725}. FT NP_BIND 402 404 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}. FT REGION 1 190 Enoyl-CoA hydratase/isomerase. FT {ECO:0000256|HAMAP-Rule:MF_01621}. FT REGION 313 719 3-hydroxyacyl-CoA dehydrogenase. FT {ECO:0000256|HAMAP-Rule:MF_01621}. FT ACT_SITE 452 452 For 3-hydroxyacyl-CoA dehydrogenase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_01621}. FT BINDING 298 298 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01621}. FT BINDING 326 326 NAD; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01621}. FT BINDING 345 345 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}. FT BINDING 409 409 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}. FT BINDING 431 431 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}. FT BINDING 455 455 NAD. {ECO:0000256|HAMAP-Rule:MF_01621}. FT BINDING 502 502 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01621}. FT SITE 120 120 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_01621}. FT SITE 140 140 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_01621}. SQ SEQUENCE 719 AA; 78134 MW; 3E1E632EAE4C89D0 CRC64; MVYQGNRITV TMLEDGIANM QYNAENESVN KFDAETNKQF GEAVTALEKA DDVKGLIVTS GKGVFIAGAD ITEFVGSFKK PESEIKDWVV GINDAFNRFE DLPFPKVAAI NGAALGGGCE MTLVCEYRVM SDKAIIGLPE TQLGIFPGFG GTVRTTRVIG IDNALELIAT GTPKKPLDAL KLGLVDATVA ADDLQDAAID LVKKCISGEL DWKAKREEKL NPVKLNQLEQ AMAFNSAKGM IFAKANPKQY PAPALAIAAM EKHVNLPRDK AIEVEAAGFA KAAKTPQAES LVGLFLSDQL VKKLAKQHSK KAHEINEAAV LGAGIMGGGI AYQAASKGLP IIMKDIKSEQ LDLGMGEASK LLGKMVDRGK MTPAKMGETL SRIRPTLNYG DFAETDIVIE AVVENPNVKR AVLKEVEGLV KDDCILASNT STISITFLAE ALERPENFVG MHFFNPVHRM PLVEVIRGEK SSEEAIATTV ALASKMGKVP VVVNDCPGFL VNRVLFPYFG AFDLLLKQGA DFAHVDKVME KFGWPMGPAY LIDVVGLDTG VHGAEVMAEG FPDRMKPDYK GAIELLYENK RLGQKNGVGF YKYEMDKRGK PKKVADEATY ELLKTTTDSD KQTFEDQAII DRTMLAFCNE TVRCLEDNIV STPSEADMAM IMGVGFPPFR GGPCRYIDQM GLDNYLALCE KYAYLGKAYE APQKIRDMAA AGDTFYATA //